Pubfacts - Scientific Publication Data
  • Categories
  • |
  • Journals
  • |
  • Authors
  • Login
  • Categories
  • Journals

Search Our Scientific Publications & Authors

Publications
  • Publications
  • Authors
find publications by category +
Translate page:

Amino acids stimulate cholecystokinin release through the Ca2+-sensing receptor.

Authors:
Yu Wang Rashmi Chandra Leigh Ann Samsa Barry Gooch Brian E Fee J Michael Cook Steven R Vigna Augustus O Grant Rodger A Liddle

Am J Physiol Gastrointest Liver Physiol 2011 Apr 23;300(4):G528-37. Epub 2010 Dec 23.

Department of Medicine, Duke University, Durham Veterans Affairs Medical Centers, Durham, North Carolina, USA.

Cholecystokinin (CCK) is produced by discrete endocrine cells in the proximal small intestine and is released following the ingestion of food. CCK is the primary hormone responsible for gallbladder contraction and has potent effects on pancreatic secretion, gastric emptying, and satiety. In addition to fats, digested proteins and aromatic amino acids are major stimulants of CCK release. However, the cellular mechanism by which amino acids affect CCK secretion is unknown. The Ca(2+)-sensing receptor (CaSR) that was originally identified on parathyroid cells is not only sensitive to extracellular Ca(2+) but is activated by extracellular aromatic amino acids. It has been postulated that this receptor may be involved in gastrointestinal hormone secretion. Using transgenic mice expressing a CCK promoter driven/enhanced green fluorescent protein (GFP) transgene, we have been able to identify and purify viable intestinal CCK cells. Intestinal mucosal CCK cells were enriched >200-fold by fluorescence-activated cell sorting. These cells were then used for real-time PCR identification of CaSR. Immunohistochemical staining with an antibody specific for CaSR confirmed colocalization of CaSR to CCK cells. In isolated CCK cells loaded with a Ca(2+)-sensitive dye, the amino acids phenylalanine and tryptophan, but not nonaromatic amino acids, caused an increase in intracellular Ca(2+) ([Ca(2+)](i)). The increase in [Ca(2+)](i) was blocked by the CaSR inhibitor Calhex 231. Phenylalanine and tryptophan stimulated CCK release from intestinal CCK cells, and this stimulation was also blocked by CaSR inhibition. Electrophysiological recordings from isolated CCK-GFP cells revealed these cells to possess a predominant outwardly rectifying potassium current. Administration of phenylalanine inhibited basal K(+) channel activity and caused CCK cell depolarization, consistent with changes necessary for hormone secretion. These findings indicate that amino acids have a direct effect on CCK cells to stimulate CCK release by activating CaSR and suggest that CaSR is the physiological mechanism through which amino acids regulate CCK secretion.

Download full-text PDF

Source
http://dx.doi.org/10.1152/ajpgi.00387.2010DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3074989PMC
April 2011

Publication Analysis

Top Keywords

amino acids
32
cck cells
24
cck
15
cck release
12
cells
11
blocked casr
8
phenylalanine tryptophan
8
intestinal cck
8
hormone secretion
8
casr
8
cck secretion
8
mechanism amino
8
aromatic amino
8
amino
8
ca2+-sensing receptor
8
acids
7
secretion
5
cells loaded
4
staining antibody
4
antibody specific
4

Keyword Occurance

Similar Publications

Effect of Penicillium candidum and Penicillium nalgiovense and their combination on the physicochemical and sensory quality of dry-aged beef.

Authors:
Yee Eun Lee Hyun Jung Lee Cho Hyun Kim Sangdon Ryu Younghoon Kim Cheorun Jo

Food Microbiol 2022 Oct 22;107:104083. Epub 2022 Jun 22.

Department of Agricultural Biotechnology, Center for Food and Bioconvergence, Research Institute of Agriculture and Life Science, Seoul National University, Seoul, 08826, South Korea; Institute of Green Bio Science and Technology, Seoul National University, Pyeongchang, 25354, South Korea. Electronic address:

This study was designed to investigate the effect of starter culture on the improvement of physicochemical and sensory properties of dry-aged beef. Penicillium nalgiovense and Penicillium candidum were used as single starter cultures and mixed suspensions (1:1) to determine the effect of mixed starter culture. Starter cultures were spray-inoculated on the surface of beef samples, and samples were dry-aged for 0, 7, 10, 14, and 21 days. Read More

View Article and Full-Text PDF
October 2022
Similar Publications

Parathyroid hormone-related protein in breast cancer bone metastasis.

Authors:
Rachelle W Johnson Julie Rhoades T John Martin

Vitam Horm 2022 11;120:215-230. Epub 2022 Jul 11.

St Vincent's Institute of Medical Research, University of Melbourne, St Vincent's Health, Melbourne, VIC, Australia. Electronic address:

Parathyroid hormone-related protein (PTHrP) was discovered as the tumor product causing the humoral hypercalcemia of malignancy. Its structural similarity to the hormone, PTH, with 8 of the first 13 amino acids identical, was sufficient to explain the sharing by PTHrP and PTH of a common receptor, PTH1R, although the remainder of the sequences are unique. PTHrP has important roles in development of several organs, including breast and bone, and functions as a paracrine factor postnatally in these and other tissues. Read More

View Article and Full-Text PDF
July 2022
Similar Publications

Parathyroid hormone-related protein (PTHrP)-dependent modulation of gene expression signatures in cancer cells.

Authors:
Claudio Luparello Mariangela Librizzi

Vitam Horm 2022 16;120:179-214. Epub 2022 May 16.

Dipartimento di Scienze e Tecnologie Biologiche, Chimiche e Farmaceutiche (STEBICEF), Università di Palermo, Palermo, Italia.

PTHrP is encoded by PTHLH gene which can generate by alternative promoter usage and splicing mechanisms at least three mature peptides of 139, 141 and 173 amino acids with distinct carboxy terminus. PTHrP may undergo proteolytic processing into smaller bioactive forms, comprising an amino terminus peptide, which is the mediator of the "classical" PTH-like effect, as well as midregion and carboxy terminus peptides that act as multifaceted critical regulator of proliferation, differentiation and apoptosis via the reprogramming of gene expression in normal and neoplastic cells. Moreover, a nuclear/nucleolar localization signal sequence is present in the [87-107] domain allowing PTHrP nuclear import and "intracrine" effect additional to the autocrine/paracrine one. Read More

View Article and Full-Text PDF
May 2022
Similar Publications

Identification of Single Amino Acid Chiral and Positional Isomers Using an Electrostatically Asymmetric Nanopore.

Authors:
Jiajun Wang Jigneshkumar Dahyabhai Prajapati Fan Gao Yi-Lun Ying Ulrich Kleinekathöfer Mathias Winterhalter Yi-Tao Long

J Am Chem Soc 2022 Aug 11. Epub 2022 Aug 11.

State Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, China.

Chirality is essential in nearly all biological organizations and chemical reactions but is rarely considered due to technical limitations in identifying L/D isomerization. Using OmpF, a membrane channel from with an electrostatically asymmetric constriction zone, allows discriminating chiral amino acids in a single peptide. The heterogeneous distribution of charged residues in OmpF causes a strong lateral electrostatic field at the constriction. Read More

View Article and Full-Text PDF
August 2022
Similar Publications

Cathepsin C (CTSC) contributes to the antibacterial immunity in golden pompano (Trachinotus ovatus).

Authors:
Qianying Diao Hehe Du Na Zhao Ying Wu Xiangyu Du Yun Sun Yongcan Zhou Zhenjie Cao

Fish Shellfish Immunol 2022 Aug 8. Epub 2022 Aug 8.

State Key Laboratory of Marine Resource Utilization in South China Sea, Hainan University, PR China; Hainan Provincial Key Laboratory for Tropical Hydrobiology and Biotechnology, College of Marine Science, Hainan University, PR China.

Cathepsins, as a class of protein hydrolases, are widely found in the lysosomes of many tissues and play an essential role in various physiological activities. Cathepsin C (CTSC), a lysosomal cysteine protease, is an essential component of the lysosomal hydrolase family. In this study, we identified a CTSC from Trachinotus ovatus (TroCTSC) and analyzed its function. Read More

View Article and Full-Text PDF
August 2022
Similar Publications
}
© 2022 PubFacts.
  • About PubFacts
  • Privacy Policy
  • Sitemap